Periplasmic Superoxide Dismutase in Meningococcal Pathogenicity: Meningococcal sodC encodes periplasmic copper- and zinc-cofactored superoxide dismutase (Cu,Zn
rdf:RDF xmlns:dcterms=http://purl.org/dc/terms/ xmlns:dc=http://purl.org/dc/elements/1.1/ xmlns:rdf=http://www.w3.org/1999/02/22-rdf-syntax-ns# xmlns:bibo=http://purl.org/ontology/bibo/ xmlns:dspace=http://digital-repositories.org/ontologies/dspace/0.1.0# xmlns:foaf=http://xmlns.com/foaf/0.1/ xmlns:void=http://rdfs.org/ns/void# xmlns:xsd=http://www.w3.org/2001/XMLSchema# , ,rdf:Description rdf:about=https://kops.uni-konstanz.de/rdf/resource/123456789/1275, ,dspace:isPartOfCollection rdf:resource=https://kops.uni-konstanz.de/rdf/resource/123456789/28/, ,dc:creator,Qu, Jian,/dc:creator, ,dc:contributor,Holst, Otto,/dc:contributor, ,foaf:homepage rdf:resource=http://localhost:8080/jspui/, ,dcterms:abstract xml:lang=eng,Periplasmic Skp facilitates folding and membrane insertion of many outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria. We have examined the binding sites of outer membrane protein A (OmpA) from Escherichia coli in its complexes ...
Periscope 20150806 :: DESCRIPTION Constructed based on the rising popularity of periplasmic expression, Periscope is a sequence-based predictor with a two-stage architecture that estimates the expression level and yi
The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(kcat/Km)/kuncat] for ampicillin hydrolysis of 2.3 × 106 and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions.. ...
b). However, the solution model of RseA121-216/RseB clearly shows that its envelope is more globular than either free RseB or the RseA169-196/RseB complex, thereby suggesting that the cleft in free RseB is occupied by a certain region of RseA. Since the minimum binding fragment (RseA169-196) was not clearly visualized in the RseA169-196/RseB complex and the empty cleft in free RseB was occupied in the complex of RseA121-216/RseB, it is thought that some other region of RseA was also involved in RseB binding and was visualized in the SAXS model of the RseA121-216/RseB complex. Taking these results together, it can be proposed that the unstructured free RseA becomes more structured and stabilized when it binds to RseB, and more than two separate regions of RseA are involved in RseB binding. Consistently with our notion, it has been proposed that the periplasmic domain of RseA would interact with RseB using two regions: residues near 169-186 and an undefined region (Cezairliyan & Sauer, 2007 ...
The different orientations of the periplasmic loop. a UreI at pH 2.0 and a zoom to the trapped conformation, facing the adjacent chain against clockwise. b Con
The separation of charge across the photosynthetic membrane is followed by microsecond/millisecond timescale reactions to generate the substrates for the cytochrome bc1 complex. On the so-called acceptor side, QA− reduces the ubiquinone at the QB site (Figure 2A), forming a singly reduced semiquinone species, while on the donor side, a reduced cytochrome c2 docks to the periplasmic face of the RC and reduces P+. The latter event reprimes the RC for a second light-induced charge separation to form the P+QA− radical pair. Donation of a second electron from QA− to the QB− semiquinone is accompanied by a double protonation of the QB molecule to form ubiquinol, which then migrates into the membrane interior and is replaced by a new ubiquinone from the intramembrane pool (Figure 2A, dotted arrows). The sequence and energetics of reduction and protonation events at the QB site have been subjected to an extremely detailed scrutiny (see [38,39] for reviews). The double reduction and protonation ...
An additional difficulty to derive functional interaction pathways is that the difference in affinity between specific and non-specific interactions has been shown to be less than two orders of magnitude in the case of SH2 and its peptide ligands [Songyang 2004]. Even when granted that the recognition specificity of intact proteins by SH3 domains is greater than for SH3-peptide recognition, affinity is not raised above one order of magnitude [Lee 1995 Oct 16; Arold 1998 Oct 20]. Moreover, the ability of a point-mutant Src SH2 domain to effectively substitute for the SH2 domain of the Sem-5 protein in activation of the Ras pathway in vivo emphasises that the specificity of Sh2-mediated interactions is not great [Marengere 1994]. Consider the later statements under the light of the fact that the affinity of the protein OppA for its ligands is in the range of two orders of magnitude (Oppa is involved in the mopping of peptides in the bacterial periplasm exhibiting no sequence specificity). Tu ...
Design. We had the LC-Cutinase gene synthesized with a pelB leader sequence and a 6-his tag (the full construct being labeled as Bba_K936014). The pelB leader sequence, when translated, is a protein tag that directs the attached protein to the periplasmic space and is removed by a pelB peptidase once in the periplasm. We used this tag as a method of protein secretion as it had been reported that once LC-cutinase was brought to the membrane, a leakage occurs that helps the catalyst to be secreted into the extracellular matrix [1]. This secretion is desirable for both the purification of the enzyme and for future applications where the bacterial culture would be directly incubated with the PET. The his-tag was included at the end of the sequence for additional purification purposes and to conduct experiments that would determine where the protein goes after production (i.e. extracellular or intracellular space). We have two different constructs expressing this part: one with a constitutive ...
Purpose: Oxidative stress is generated through imbalance between composing and decomposing of reactive oxygen species (ROS). This kind of stress was rarely discussed in connection with foreign protein production in Escherichia coli. Effect of cytoplasmic recombinant protein expression on Hydrogen peroxide concentration and catalase activity was previously reported. In comparison with cytoplasm, periplasmic space has different oxidative environment. Therefore, in present study we describe the effect of periplasmic expression of recombinant human interleukin-2 (hIL-2) on ...
RseB from Escherichia coli has been crystallized and crystal structures were determined at 2.4 Å and at 2.8 Å resolution. The structure of cytoplasmic expressed RseB revealed that it consists of two domains; an N-terminal large and a C-terminal small domain. The large domain resembles an unclosed β-barrel that is structurally remarkably similar to a protein family (LolA, LolB) capable of binding the lipid anchor of lipoproteins. Detailed structural comparison of RseB and LolA led to the hypothesis that RseB might be a sensor for mislocalized lipoproteins. The small C-terminal domain, connected to the large domain by a partially unstructured loop, was identified to mediate interaction with RseA. A peptide comprised of a putative helix of RseA was shown to constitute the binding site for RseB. Structure based results presented in this thesis indicate a new role of RseB in acting as a sensor for periplasmic stress: it detects mislocalized lipoproteins in the periplasm and propagates the signal ...
where rc is the rate of conformational change.. The rates of conformational change on the periplasmic side, measured in DDM by unquenching of Trp introduced at the periplasmic gate of the N245W/A155C mutant, are 50-100 s-1 for different galactosidic sugars (Fig. 7, open symbols). The rate of Trp unquenching is relatively slow and depends marginally on sugar concentration, although the affinities of LacY for these sugars and the non-galactosyl moieties differ markedly (25) (see Fig. S7C). Essentially the same rate is observed for NPG binding with reconstituted N245W/A155C, and it is also independent of sugar concentration. Therefore, the rate of opening of the periplasmic cavity is evidently a limiting step in the sugar-binding process. Sugar binding in proteoliposomes is likely to represent the rate of spontaneous opening of the periplasmic cavity in the absence of substrate, whereas unquenching of Trp245 in detergent solution represents the rate of opening induced by bound sugar. However, both ...
Shop Nopaline-binding periplasmic protein ELISA Kit, Recombinant Protein and Nopaline-binding periplasmic protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
The periplasmic space between the cell membrane and the cell wall is of key interest in this project, as it is where the final stages of PG synthesis occur and where penicillin acts. Our main objective is to understand how this periplasmic space is maintained when it would be expected that turgor would force the cytoplasmic membrane against the PG layer. This will further allow us to explore the effects of antibiotics on the maintenance of the bacterial periplasm ...
Autophosphorylation of CpxA is stimulated by multiple stimuli, such as alkaline pH, altered membrane lipid composition, interaction with hydrophobic surfaces, and high osmolarity, among others [26]. NlpE, an outer membrane lipoprotein, when overexpressed also stimulates the activity of CpxA [29] and is required for the activation of CpxA in response to adherence to hydrophobic surfaces [30] or external copper ions [31], or in the presence of oxidative folding defects [32]. When the C-terminal domain of NlpE does not contain a disulfide bond, the N-terminal domain of NlpE appears to interact directly with the periplasmic domain of CpxA to turn on the cpx system [32]. The autokinase activity of CpxA is inhibited by CpxP, a small periplasmic protein that binds to the periplasmic domain of CpxA [33]. This small protein is degraded in turn by the protease DegP in response to PapE/PapG misfolding or to alkaline pH [34, 35]. CpxR activates both the cpxP and degP genes [3]. When CpxA is phosphorylated, ...
If the gene of interest is also being translated, then RFP should also be translated because it is fused to the GOI.the RFP was specially selected from Dr. Lewenzas lab. This RFP (nicknamed sRFP or special red fluorescent protein) can fold in the cytoplasm, periplasm and the cellular membrane. PICTURE GOES HERE; RED PLATE Assumptions:. For this circuit to work, there are several assumptions that must be made. The first of which is a result of a limitation within the design which is that sRFP will not affect the stability of the protein of interest. Both positives and negatives are not ideal because the circuit functions as an indicator any assistance could lead to false positives or vice versa. Second, AraC is the right promoter for this circuit. Although there are many benefits for using an arabinose inducible promoter, however evolutionary conditions have established optimal expression in natural promoters. Third is folding properties in the periplasm and cytoplasm (Lewenza, et al., 2006) had ...
To date, the only proteins implicated in LPS transport are MsbA (TC# 3.A.1.106), responsible for LPS flipping across the inner membrane, and the Imp/RlpB complex, involved in LPS targeting to the OM. Two additional Escherichia coli essential genes, yhbN and yhbG, renamed lptA and lptB, respectively, participate in LPS biogenesis (Sperandeo et al., 2007). Mutants depleted of LptA and/or LptB not only produce an anomalous LPS form, but also are defective in LPS transport to the OM and accumulate de novo-synthesized LPS in a novel membrane fraction of intermediate density between the inner membrane (IM) and the OM. LptA is located in the periplasm, and expression of the lptA-lptB operon is controlled by the extracytoplasmic σ factor RpoE. LptA and LptB are implicated in the transport of LPS from the IM to the OM of E. coli, possibly together with Imp/RlpB. A unique LptA structure reported by Suits et al (2008) represents a novel fold, consisting of 16 consecutive antiparallel beta-strands, folded ...
A structure that lies outside the plasma membrane and surrounds the entire cell or cells. This does not include the periplasmic space. [GOC:go_curators]. ...
MetabolismTransport and binding proteinsAmino acids, peptides and amineslysine-arginine-ornithine-binding periplasmic protein (TIGR01096; HMM-score: 22.2) ...
Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism.
UreB is one of the urease subunits of Helicobacter pylori and can be used as an excellent antigen candidate for H. pylori vaccination. Easy access to highl
TY - JOUR. T1 - Periplasmic chaperone recognition motif of subunits mediates quaternary interactions in the pilus. AU - Soto, Gabriel E.. AU - Dodson, Karen W.. AU - Ogg, Derek. AU - Liu, Christopher. AU - Heuser, John. AU - Knight, Stefan. AU - Kihlberg, Jan. AU - Jones, C. Hal. AU - Hultgren, Scott J.. PY - 1998/11/2. Y1 - 1998/11/2. N2 - The class of proteins collectively known as periplasmic immunoglobulin-like chaperones play an essential role in the assembly of a diverse set of adhesive organelles used by pathogenic strains of Gram-negative bacteria. Herein, we present a combination of genetic and structural data that sheds new light on chaperone-subunit and subunit-subunit interactions in the prototypical P pilus system, and provides new insights into how PapD controls pilus biogenesis. New crystallographic data of PapD with the C-terminal fragment of a subunit suggest a mechanism for how periplasmic chaperones mediate the extraction of pilus subunits from the inner membrane, a ...
McNulty, BC, Young, GB, Pielak, GJ. 2006. Macromolecular crowding in the Escherichia coli periplasm maintains α-synuclein disorder. Journal of Molecular Biology, 355: 893-897.. McNulty, B. C., Tripathy, A., Young, G. B., Orans, J., Charlton, L. M. and Pielak, G. J. (2006) Temperature- Induced Reversible Conformational Change in the First 100 Residues of Alpha-Synuclein. Protein Science 15:602-608.. Lentz, BR. 2006. Seeing is Believing: the Stalk Intermediate. Biophysical Journal, 91, 2747-8, 2006 (mini-review to highlight a recent BJ paper).. 2005. Kevin A. Wilkinson, Edward J. Merino, and Kevin M. Weeks. 2005. RNA SHAPE Chemistry Reveals Nonhierarchical Interactions Dominate Equilibrium Structural Transitions in tRNA Asp Transcripts. J. Am. Chem. Soc. 127:4659-4667.. Ortlund, EA, Lee, Y, Solomon, IH, Hager, JM, Safi, R, Choi, Y, Guan, Z, Tripathy, A, Raetz, CR, McDonnell, DP, Moore, DD, Redinbo, MR. 2005. Modulation of human nuclear receptor LRH-1 activity by phospholipids and SHP. Nat Struct ...
Unicellular Organisms: Eubacteria, Archea, Yeast Lecture 27, Chapter 21 May 13, 2004 Jeff Esko. Overview. General structure of bacterial cell walls Structure, function and assembly of peptidoglycan (murein) Periplasmic  -glucans (MDO) Lipopolysaccharide (LPS) - endotoxin Slideshow...
Shop Molybdate-binding periplasmic protein ELISA Kit, Recombinant Protein and Molybdate-binding periplasmic protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Condon SGF, Deena-Al M, Armstrong CR, Diaz-Vazquez G, Craven SJ, LaPointe LM, Khadria AS, Chadda R, Crooks JA, Rangarajan N, et al. The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions. Journal of Biological Chemistry. 2018 ;293:1623-1641. ...
Archaea, one of three domains of life, rotate archaella for swim. How periplasmic components of archaellum contributing to motility is not clear.
Universal BiGG reaction 2AGPA120tipp. 2-Acyl-sn-glycero-3-phosphatidate (n-C12:0) transporter via facilitated diffusion (periplasm).
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The vascular wilt fungi Verticillium dahliae and V. albo-atrum infect over 200 plant species, causing billions of dollars in annual crop losses. The characteristic wilt symptoms are a result of colonization and proliferation of the pathogens in the xylem vessels, which undergo fluctuations in osmolarity. To gain insights into the mechanisms that confer the organisms pathogenicity and enable them to proliferate in the unique ecological niche of the plant vascular system, we sequenced the genomes of V. dahliae and V. albo-atrum and compared them to each other, and to the genome of Fusarium oxysporum, another fungal wilt pathogen. Our analyses identified a set of proteins that are shared among all three wilt pathogens, and present in few other fungal species. One of these is a homolog of a bacterial glucosyltransferase that synthesizes virulence-related osmoregulated periplasmic glucans in bacteria. Pathogenicity tests of the corresponding V. dahliae glucosyltransferase gene deletion mutants ...
Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism.
Background Chorismate mutases of the AroQ homology class are widespread in the Bacteria and the Archaea. Many of these exist as domains that are fused with other aromatic-pathway catalytic domains. Among the monofunctional AroQ proteins, that from Erwinia herbicola was previously shown to have a cleavable signal peptide and located in the periplasmic compartment. Whether or not this might be unique to E. herbicola was unknown. Results The gene coding for the AroQ protein was cloned from Salmonella typhimurium, and the AroQ protein purified from both S. typhimurium and Pseudomonas aeruginosa was shown to have a periplasmic location. The periplasmic chorismate mutases (denoted *AroQ) are shown to be a distinct subclass of AroQ, being about twice the size of cytoplasmic AroQ proteins. The increased size is due to a carboxy-terminal extension of unknown function. In addition, a so-far novel aromatic aminotransferase was shown to be present in the periplasm of P. aeruginosa. Conclusions Our analysis has
Three anti-ABA single-chain Fv (scFv) antibody genes, namely ABA26, MAC61, MAC252 scFvs, had been constructed from mouse and rat hybridomas and expressed in bacteria, yeast and plants. All of these scFv genes could be expressed in E. coli using the T7 promoter, either targeted to the E. coli periplasm or cytoplasm, albeit at comparatively low levels. The cytoplasmically located scFv proteins were in the form of insoluble fraction and did not therefore exhibit any binding activities to the ABA. The majority of the periplasmically located scFv proteins were retained in the bacterial cytoplasm as insoluble bodies with the ompA signal peptide attached to them. Nevertheless, the positive signal in ELISA test indicated that a small portion of scFv proteins were in the form of soluble functional scFv proteins. All the three periplasmically expressed scFv proteins had specific ABA binding activities. However, the affinity constants of the scFv proteins were found to be 5 to 10 fold lower than those of ...
We cloned, overexpressed, purified, and characterized HdeB as a novel acid stress chaperone. HdeB was found in the periplasm in a soluble form. It was purified by osmotic shock, followed by two chromatographic steps on DEAE-Sephacel and hydroxyapatite columns, and identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry. We purified HdeA in parallel in order to compare the two chaperones.. A periplasmic extract from the hdeB mutant aggregated at pH 2 and pH 3, like an extract from the hdeA mutant (9). The aggregation defect of the hdeB mutant did not result from the lower expression (24% of the wild-type level) of HdeA, since complementation of this mutant by the HdeA expression plasmid did not rescue its aggregation defect. Thus, HdeB is important for the solubility of the bacterial periplasm at acidic pH.. At pH 2, HdeA is the main chaperone involved in the in vitro solubilization of periplasmic extracts and of the model substrate proteins used in our study ...
The mxiM locus of S. flexneri encodes a secreted protein with no detectable homologs among other type III secretion systems (4). Recent BLAST and FASTA searches have also failed to detect proteins with similarities to MxiM (data not shown). Since homologs have been detected for the majority of Mxi-Spa proteins, MxiM may be required for functions specific toShigella. Of particular interest to us was the work of Allaoui et al. (4) which showed that a MxiM-PhoA hybrid protein is lipid modified (and detectable in whole-cell protein extracts). Recent work has implicated bacterial lipoproteins as essential subunits of most transmembrane traffic systems. Therefore, while it is not a component commonly found among type III secretory pathways, MxiM is likely to play an important, if not essential, role in the pathway for Ipa secretion.. In this study we characterized the contribution of MxiM to the virulent phenotype of Shigella, using a combination of genetic and biochemical analyses. By allelic ...
thoroughly and pour plates. YEPD (YPD) PLATES: Agar 20 g. Peptone 10 g. Yeast Extract 900 ml distilled water: 5 ml of 1 M HCl (do not mouth pipette) 20 g. Agar Autoclave.Préparation de membranes pour. Ampicilline A~P 100 Carbeniciline Cb 40 Kanam ycine Km 20. - Milieu LB agar:.Lb agar with ampicillin, ampicillin agar plates - wwgcsa. What is the best ampicillin to chloramphenicol ratio for.. TP biorad (B)TP sauce Paul Éluard (PE) Jour 1 Préparation de 8 milieux LB (B)Couler. Ampicilline et Arabinose. de soja 5 g Chlorure de sodium 5 g Agar.Periplasmic Expression of a Novel Human Bone Morphogenetic Protein-7 Mutant in. of a Novel Human Bone Morphogenetic Protein-7 Mutant in. in LB agar and LB Broth.Préparation de la recette: Râpez la plaquette de chocolat blanc en fins copeaux ou hachez-la à laide dun couteaux-scie. Rassemblez les copeaux dans un saladier.Inoculum and plasmid preparation. [LB] medium) overnight,. (LB medium containing, per liter, ampicillin, 100 mg;.Préparation du milieu ...
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1OFG: The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.. ...
MetabolismTransport and binding proteinsCations and iron carrying compoundsnickel ABC transporter, nickel/metallophore periplasmic binding protein (TIGR02294; HMM-score: 784.7) ...
Editor Nick Wakeman shares six questions he plans to ask during a roundtable discussion on lowest price, technically acceptable contracting, the dreaded LPTA. Is he taking the conversation in the right direction?
The inability to form disulfide bonds in the periplasm affects the assembly of complex machinery in the cell envelope. Indeed, loss of DsbA, the primary disulfide bond oxidase in the periplasm, has been shown to block type III secretion in serovar Typhimurium, S. flexneri, P. aeruginosa, and Y. pestis and motility in E. coli and serovar Typhimurium (10, 18, 28, 34, 48, 64) (Fig. 5). But does loss of function indicate a simple defect in assembly? Here we have shown that, in addition to a structural or functional defect conferred by mutations in dsbA, there is a distinct regulatory response. The SPI1 T3SS regulatory circuit responds to the state of disulfide bonds in the periplasm and adjusts expression of the machine components. Our results suggest that loss of DsbA affects SPI1 through four distinct yet overlapping pathways (Fig. 1). First, DsbA inhibits activation of the RcsCDB system (45). Activation of RcsCDB in a dsbA mutant inhibits hilA expression (50) through HilD. Activated RcsCDB also ...
Considerable insight has been gained on Periplasmic Binding proteins from E.coli as novel candidates to develop sensors for metabolites like glucose, glutamine and lactate. However, these proteins are still used as assays and for them to become sensors and used repeatedly, require immobilization. Additionally, there is not much information on the application of the sensors in combination with innovative sampling technologies. The first part of the research deals with constructing C- terminal Poly histag Glucose/Galactose binding protein and C-terminal Poly histag lactate binding protein and evaluating their sensing properties. Histag serve the purpose of purification and immobilization of these proteins. Secondly, the application of the Glutamine binding protein form E.coli as a potential sensor to measure glutamine in Mammalian cell cultures in High throughput bioreactors has been shown. Sampling has been done by microdialysis which is a fast and reliable technique. These histagged proteins ...
Domain combinations containing the Periplasmic binding protein-like I superfamily . Domain architectures illustrate each occurrence of the Periplasmic binding protein-like I superfamily.
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4HBR: Crystal structure of a putative periplasmic proteins (BACEGG_01429) from Bacteroides eggerthii DSM 20697 at 2.40 A resolution
5.B.11. The One Electron Transmembrane Transfer Complex (TmcABCD) Family Pereira et al. 2006 reported that three membrane-bound redox complexes are present in Desulfovibrio spp., whose genes are not found in the genomes of other sulfate reducers such as Desulfotalea psycrophila and Archaeoglobus fulgidus. These complexes contain a periplasmic cytochrome c subunit of the cytochrome c3 family, and their presence in these organisms correlates with the presence of a pool of periplasmic cytochromes c3, also absent in the two other sulfate reducers. Pereira et al. 2006 isolated and characterized the first of such complexes, Tmc from D. vulgaris Hildenborough, which is associated with the tetraheme type II cytochrome c3. The isolated Tmc complex contains four dissimilar subunits, including the small TpIIc3 (TmcA), an integral membrane cytochrome b (TmcC), and two cytoplasmic proteins, an iron-sulfur protein (TmcB) and a tryptophan-rich protein (TmcD). Spectroscopic studies indicated the presence of ...
The production of biotherapeutics including antibodies and antibody fragments is a rapidly expanding market with an increasing number of products being approved for use. One of the major platforms used for production of such therapeutics is Escherichia coli, which offers a rapid production at low production costs. The favoured location for targeting these biotherapeutic is the periplasm of E. coli as this environment supports the formation of disulphide bonds and simplifies the purification process. There are a number of periplasmic release procedures currently practised in industry including osmotic shock. However their limitations call for the development of an improved generic periplasmic release method ...
Bacteria outer membrane lipoprotein I: vaccine candidate; antigenically cross-reacts with all serotype strains of the International Antigenic Typing Scheme; amino acid sequence given in first source
The periplasm (the space between the inner and outer membranes of bacteria) is the site of activation of the periplasmic stress response. Like the cytosolic stress response and the eukaryotic endoplasmic and cytosolic stress responses, unfolded proteins trigger a transcriptional activation profile that allows cells to produce more chaperones and protein-folding agents (see Young and Hartl). Although, the periplasmic stress response is fairly well characterized, the sensor that initiates the process has remained elusive. The response consists of activation of the protease DegS, which cleaves transmembrane protein RseA, which then releases the transcription factor σE to allow the activation of stress response genes. Walsh et al. show that DegS is inhibited by its PDZ domain and that binding of the PDZ domain toYQF motifs of outer membrane protein porins activates the protease. Bacteria expressing DegS lacking the PDZ domain showed increased σE activity. Using an oriented peptide library, a ...
Protein TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy- requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (249 aa ...
FDHA_METFO (P06131 ), FDHA_METJA (P61159 ), FDHF_ECOLI (P07658 ), FDHL_STAA3 (Q2FEI5 ), FDHL_STAA8 (Q2FVV9 ), FDHL_STAAB (Q2YYT1 ), FDHL_STAAC (Q5HDP9 ), FDHL_STAAM (Q931G2 ), FDHL_STAAN (Q99RW4 ), FDHL_STAAR (Q6GEC4 ), FDHL_STAAS (Q6G711 ), FDHL_STAAW (Q7A057 ), FDHL_STAHJ (Q4L8G8 ), FDHL_STAS1 (Q49ZN0 ), FDNGA_DESVH (Q727P3 ), FDNG_ECOLI (P24183 ), FDOG_ECOLI (P32176 ), FDXG_HAEIN (P46448 ), NAPA1_PHOPR (Q6LTV9 ), NAPA2_PHOPR (Q6LQJ3 ), NAPA_ACTP2 (A3N277 ), NAPA_ACTP7 (B3H2D1 ), NAPA_ACTPJ (B0BR28 ), NAPA_ACTSZ (A6VQY7 ), NAPA_AERHH (A0KIM1 ), NAPA_AERS4 (A4SPG7 ), NAPA_AGGAC (Q8VL02 ), NAPA_AGRFC (Q8U7P1 ), NAPA_BORBR (Q7WIQ1 ), NAPA_BORPA (Q7W733 ), NAPA_BORPD (A9I7M5 ), NAPA_BRADU (Q89EN5 ), NAPA_BRASB (A5ED21 ), NAPA_BRASO (A4Z0A1 ), NAPA_CAMC1 (A7ZCK4 ), NAPA_CAMC5 (A7GZP5 ), NAPA_CAMFF (A0RQ36 ), NAPA_CAMHC (A7I3Y7 ), NAPA_CAMJ8 (A8FLJ3 ), NAPA_CAMJE (Q9PPD9 ), NAPA_CAMJJ (A1VZC8 ), NAPA_CAMJR (Q5HV12 ), NAPA_CAMLR (B9KCQ2 ), NAPA_CITK8 (A8AE11 ), NAPA_COLP3 (Q487G4 ), NAPA_CUPNH ...
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Kevser G lcihan Balc , Orhan Maden, Mustafa M cahit Balc , Fatih en, Sefa nal, Serdar Kuyumcu, Meryem Kara, Hatice Sel uk, Mehmet Timur Selcuk, Ahmet ...